The overall objective of this work is to describe in detail the structure-function biochemistry of bacterial neuraminidases. The immediate goal is to continue our efforts to characterize the physical and chemical properties of homogeneous neuraminidase obtained from Arthrobacter sialophilum. The mechanism of action of this enzyme will be investigated by determining the amino acid residues at the active site by the use of conventional group-specific and novel site-directing irreversible inhibitors. The latter compounds may also have potential chemotherapeutic value in the treatment of such infectious diseases as influenza and bacterial pneumonia. The physical and chemical properties of immobilized neuraminidase will be determined and compared to those of the free enzyme. The factors controlling the induction of neuraminidase in A. sialophilum will be determined. BIBLIOGRAPHIC REFERENCES: Properties of Arthrobacter Neuraminidase, M. Flashner, P. Wang, and S.W. Tanenbaum, FASEB, 35, 1667 (1976). "Biochemical Properties of Arthrobacter Neuraminidase", Philip Wang, Stuart W. Tanenbaum, and Michael Flashner, 7th Northeast Regional Meeting American Chemical Society, 149 (1976).